A0A8K1ZY90 · A0A8K1ZY90_9CYAN

Function

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

  • Hydrolysis of oligopeptides, with broad specificity. Gly or Ala commonly occur as P1 or P1' residues, but more distant residues are also important, as is shown by the fact that Z-Gly-Pro-Gly-|-Gly-Pro-Ala is cleaved, but not Z-(Gly)5.
    EC:3.4.24.70 (UniProtKB | ENZYME | Rhea)

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Molecular Functionmetal ion binding
Molecular Functionmetalloendopeptidase activity
Biological Processpeptide metabolic process
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    oligopeptidase A
  • EC number

Gene names

    • ORF names
      GS597_06200

Organism names

  • Taxonomic identifier
  • Strain
    • C
  • Taxonomic lineage
    Bacteria > Cyanobacteriota > Cyanophyceae > Synechococcales > Petrachlorosaceae > Petrachloros > Petrachloros mirabilis

Accessions

  • Primary accession
    A0A8K1ZY90

Proteomes

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain32-154Oligopeptidase A N-terminal
Domain234-696Peptidase M3A/M3B catalytic

Sequence similarities

Belongs to the peptidase M3 family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    700
  • Mass (Da)
    78,201
  • Last updated
    2022-08-03 v1
  • Checksum
    C117F4CC33D6F1B9
MTGTAIAANPLLQGKGLPPFDQMQPEHVVPAMTQLLQELEQALNELETQVTPTWDGLVEPLEHLGERLRWSWGVVGHLMGVKNSPELRQAYEAVQPQVVEFSNRLSQSRPLYEAFKAMAASDQWAQFQPAQQRIIETAILDAELSGVGLTGEAKERFNAIQLELANLSTTFSNHVLDATNAFSLTLTETAEVEGLPPSLLSFAAQSAREAGHEDATTESGPWRITLDFPSFGPFLQHSRRRDLREKVYRAYISRASAGEYDNTPLIERILALRQEEAQLLGYDSYAEVSLAAKMAPSVDAVEKLMEDLRQASYDAAVQDLDTLKAFAASKGAPEATDLKHWDISFWAERQREEKFTLTDEQLRPYFPLPQVLEGLFTLVHRLFGVTVTAADGAAPVWHPDVRYFQIADERDTVIAHFYLDPYSRPAEKRGGAWMDECLGRGQWHQPDGSTKIQLPVAYLVCNQTPPVEGKPSLMTFREVETLFHEFGHGLHHMLTQVDFAGAAGINNVEWDAVELPSQFMENWCYDHATLMGMARHYETGEPLPEEYYERLVAARTYMSGTATLRQLHFSWVDLELHDRYGSDGDETISQVRHRLAKTTTVLPPLPEDAFLCSFGHIFAGGYAAGYYSYKWAEVLSADAFAAFEEAGLEDEAAIATTGRRFRETVLALGGSQPPMEIFKAFRGREPSTEALLRHSGLVAA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WVIC01000009
EMBL· GenBank· DDBJ
NCJ06113.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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